Fc-Fusion Development

Overview of Fc-fusion Based Half-Life Extension

IgG molecules of the IgG1, IgG2, and IgG4 subclasses exhibit exceptionally long half-lives due to FcRn-mediated recycling. Half-lives of up to 4 weeks have been described for therapeutic antibodies. The binding site for FcRn resides in the Fc region is formed by the CH2 and CH3 domains. Thus, fusion to an Fcγ region endows a therapeutic protein with the half-life extension properties (increased size, FcRn recycling) of immunoglobulins. Fc fusion represents one of the most clinically successful half-life extension strategies to date and has been used in the development of a major portion of the fusion proteins. A wide range of molecules, from small peptides to larger proteins are suitable for fusion to the Fc region, suitable molecules include hormones, growth factors, blood proteins, and protein or peptide mimetics.

The role of Fc-fusion in drug half-life extension is self-evident. With experience accumulated from years of practice, Creative Biolabs has established a comprehensive technology platform offering one-stop Fc-fusion development services. Our services include but are not limited to:

Synthesizing the gene encoding the Fc-fused protein

Amplifying the gene encoding the Fc-fused protein

Construction of Fc-fusion proteins

Expression of Fc-fusion proteins

Purification of Fc-fusion proteins

If you are interested in Fc-fusion protein development services, or you have any trouble with half-life extension drugs, please feel free to contact us for more information.